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Enzymes
Globular proteins that work as catalysts by speeding up chemical reactions without being altered themselves
Substrates
substances that bind to enzymes and are then converted into products
Active site
a special region on the surface of the enzyme to which substances bind to
Enzyme-substrate complex
Temporary complex formed when substrates bind to enzymes
Enzyme-substrate specificity
The shapes and chemical properties of an enzyme and its substrate are complementary. Therefore, only one substrate can bind to an active site, which means that the active site of an enzyme can only catalyze one biochemical reaction
Define and describe enzyme activity
The catalysis of a biochemical reaction by an enzyme
Substrate binds to the active site of the enzyme (some have two substrates that bind to different parts of the active site)
While the substrates are bound to the active site, they change into different chemical substances, becoming the reaction products
Products separate from the active site, leaving it vacant for substrates to bind again
Types of enzyme-catalyzed reactions
Catabolic or anabolic
Catabolic enzyme-catalyzed reaction
A single substrate is drawn into the active site and broken apart into two or more distinct molecules
Anabolic enzyme-catalyzed reaction
Two or more substrates are held in the active site, forming bonds between them and releasing a single product
Collision
The coming together of a substrate molecule and an active site
Purpose of collision
Collisions are necessary for the substrate to bind to the active site
How does collision occur?
In most reactions, the substrates are dissolves in water around the enzyme. In liquids, particles are in continual random motion. Collisions occur because of the random movement of both substrate and enzyme
Random movement of enzymes vs substrates
Both are able to move, though most substrates are smaller than the enzyme so their movement is faster
Successful collisions
Those in which the substrate and active site are correctly aligned to allow binding to take place
Factors affecting enzyme activity
Temperature, pH and substrate concentration
How does temperature affect enzyme activity?
When heated, the particles in the liquid are given more kinetic energy. Both enzyme and substrate move around faster. Chance of substrate molecule colliding with the active site of the enzyme increases. Therefore, enzyme activity increases
When heated, bonds in the enzyme vibrate more and the chance of the bonds breaking increases. Bond breaking causes the enzyme to denature, including its active site, so it is no longer able to catalyze reactions. As more enzymes in a solution become denatured, enzyme activity falls and eventually stops
Draw a graph of temperature vs rate of reaction
As temperature increases, so does the rate of reaction. However, as the temperature increases past the optimum point, the rate of reaction falls
How does pH affect enzyme activity?
Each enzyme has an optimum pH, which is the pH at which enzyme activity is highest
When [H+] is higher or lower than the optimum, the structure of the enzyme is altered, including the active site. At a very high or low pH, most enzymes are denatured, so it no longer catalyzes the reaction
Draw a graph of pH vs enzyme activity
As pH increases, so does enzyme activity. However, as pH increases or decreases from the optimum, enzyme activity falls
How does substrate concentration affect enzyme activity?
If substrate concentration increases, substrate-active site collision will take place more frequently, and the rate at which the enzyme catalyzes the reaction increases
After the binding of a substrate to an active site, the active site is occupied and unavailable to other substrates until the product has been formed and released
As substrate concentration rises, more active sites are occupied at any moment. Consequently, more substrate-active site collisions are blocked
Hence, the increases in rate of catalysis get smaller as concentration rises
Draw a graph of substrate concentration vs enzyme activity
As substrate concentration increases, so does enzyme activity. However, the curve rises less and less steeply, but never reaches a maximum
Catalase
One of the most widespread enzymes that catalyzes the conversion of hydrogen peroxide (a toxic byproduct of metabolism) into water and oxygen
Immobilized enzymes
Enzymes attached to another material or into aggregations, so that enzyme movement is restricted
Methods of enzyme immobilization
Attaching enzymes to a glass surface
Trapping them in an alginate gel
Bonding them together to form enzyme aggregates of up to 0.1mm diameter
Advantages of immobilized enzymes
Enzymes can easily be separated from the products of the reaction, stopping the reaction at the ideal time and preventing contamination of products
Enzymes can be recycled after being retrieved from the reaction mixture, saving costs as many enzymes are very expensive
Immobilization increases the stability of enzymes to changes in temperature or pH, reducing the rate at which they are degraded and have to be replaced
Substrates can be exposed to higher enzyme concentrations than dissolved enzymes, speeding up reactions
Lactose
sugar naturally present in milk
Lactase
Enzyme that converts lactose into glucose and galactose
How is lactase obtained?
Obtained from a type of yest that grows naturally in milk. Biotech companies culture the yeast, extract the lactase and purify for sale
Advantages of lactase in food processing
Reduces lactase in milk, allowing lactose-intolerant people to consume it
Galactose and glucose are sweeter than lactose, so less sugar needs to be added to sweet foods containing milk
Lactose tends to crystallize during the production of ice cream, giving it a gritty texture. Glucose and galactose are more soluble than lactose, so they remain dissolved, giving a smoother texture
Bacteria ferment glucose and galactose more quickly than lactose, so the production of yogurt and cottage cheese is faster